title: Competition of zinc(II) with cadmium(II) or mercury(II) in binding to a 12-mer peptide.
abstract: Speciation of the complexes of zinc(II) with a dodecapeptide (Ac-SCPGDQGSDCSI-NH2), inspired by the metal binding domain of MerR metalloregulatory proteins, have been studied by pH-potentiometric titrations, UV, SRCD (synchrotron radiation circular dichroism) and (1)H NMR experiments. (MerR is a family of transcriptional regulators the archetype of which is the Hg(2+)-responsive transcriptional repressor-activator MerR protein.) The aim of the ligand-design was to retain the advantageous metal binding features of MerR proteins in a model peptide for the efficient capture of toxic metal ions. The peptide binds zinc(II) via two deprotonated Cys-thiol groups and one of the Asp-carboxylates in the ZnL parent complex, possessing a remarkably high stability (logK=9.93). In spite of the relatively long peptide loop, bis-complexes are also formed with the metal ion under basic conditions. In a competition with cadmium(II) or mercury(II), zinc(II) cannot prevent the binding of toxic metal ions by the thiolate donor groups of the ligand. Around neutral pH one equivalent of mercury(II) was shown to fully replace zinc(II) from the ZnL species. Partial replacement of zinc(II) from the peptide by one equivalent of cadmium(II), relative to zinc(II) and the ligand, is also presumable, nevertheless, spectroscopic data may suggest the formation of mixed metal ion complexes, as well. Based on the obtained results the investigated dodecapeptide can be a promising candidate for capturing toxic metal ions in practical applications.
authors.affiliation: Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, Szeged H-6720, Hungary. jancso@chem.u-szeged.hu
authors.forename: Attila
authors.initials: A
authors.lastname: Jancsó
authors.forename: Béla
authors.initials: B
authors.lastname: Gyurcsik
authors.forename: Edit
authors.initials: E
authors.lastname: Mesterházy
authors.forename: Róbert
authors.initials: R
authors.lastname: Berkecz
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D001667:Binding, Competitive; D002104:Cadmium / Q000737:chemistry* / Q000302:isolation & purification; D002413:Cations, Divalent; D002942:Circular Dichroism; D056831:Coordination Complexes / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008628:Mercury / Q000737:chemistry* / Q000302:isolation & purification; D018716:Molecular Mimicry; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D011485:Protein Binding; D014874:Water Pollutants, Chemical / Q000737:chemistry* / Q000302:isolation & purification; D015032:Zinc / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D002413:Cations, Divalent; D056831:Coordination Complexes; D004268:DNA-Binding Proteins; D008024:Ligands; C051124:MerR protein, Bacteria; D009842:Oligopeptides; D014874:Water Pollutants, Chemical; D002104:Cadmium; D008628:Mercury; D015032:Zinc
keywords: Competition; Peptide complexes; Solution studies; Toxic metal ions; Zinc(II)